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Apolipoprotein E isoprotein-specific interactions with tissue plasminogen activator.

Susan J Biehle¹, Janice Carrozzella, Rakesh Shukla

¹Department of Neurology, University of Cincinnati Medical Center, ML 0536, OH 45267-0536, USA. Susan.Biehle@uc.edu

Biochimica Et Biophysica Acta

|July 28, 2004

Summary

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Apolipoprotein E (Apo E) isoprotein-specific interactions with tissue plasminogen activator (tPA) were investigated. Apo E2, but not E3 or E4, showed significant conformational changes upon interaction with tPA, impacting biological processes.

Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Apolipoprotein E (Apo E) is a key genetic risk factor for neurological, vascular, and cardiovascular diseases.
Previous studies indicated Apo E isoprotein-specific modulation of tissue plasminogen activator (tPA) in vitro.

Purpose of the Study:

To investigate the conformational changes of Apo E isoforms (E2, E3, E4) when interacting with tPA.
To determine if tPA induces conformational changes in Apo E isoforms.

Main Methods:

Circular dichroism (CD) spectroscopy to analyze protein structure.
Dual polarization interferometry (DPI) to study molecular interactions.
In vitro assays using immobilized tPA and lipidated Apo E isoforms.

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Main Results:

Apo E2 exhibited significant, isoprotein-specific conformational changes upon interaction with immobilized tPA, unlike Apo E3 and E4.
Tissue plasminogen activator (tPA) induced changes in the helicity of lipidated Apo E2.
No detectable conformational changes were observed for Apo E3 or E4 in the presence of tPA.
Statistical analysis (Tukey's test) confirmed a significant interaction (P < 0.001) between tPA and lipidated Apo E2.

Conclusions:

The findings reveal isoprotein- and state-specific intermolecular interactions between Apo E isoforms and tPA.
These interactions, particularly with Apo E2, may elucidate the mechanisms behind Apo E's role in diseases involving blood clotting, proteolysis, and perfusion.